It is our aim to examine the nature of the metal ion and phospholipid specificity in activation of the coagulation proteins; prothrombin, factor VII, factor IX, and factor X. In this study, we will utilize fluorescence, NMR, and calorimetric techniques to evaluate the properties of various combinations of synthetic phospholipid vesicles, as well as serum lipoproteins, which are important for interaction with the various blood coagulation zymogens, and their activated forms. We will also attempt to identify, and distinguish between the various classes of metal sites on these proteins, in order that their various roles in metal binding and phospholipid binding can be evaluated. Finally, we propose to determine the carbohydrate structures of factor IX and factor X, and to initiate studies aimed at a critical examination of the role of the large amount of carbohydrate, present on factor IX and factor X, in the structure, function, and activation of these coagulation zymogens.